Solution structure of a protein denatured state and folding intermediate
β Scribed by Religa, T. L.; Markson, J. S.; Mayor, U.; Freund, S. M. V.; Fersht, A. R.
- Book ID
- 109894846
- Publisher
- Nature Publishing Group
- Year
- 2005
- Tongue
- English
- Weight
- 767 KB
- Volume
- 437
- Category
- Article
- ISSN
- 0028-0836
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It has been shown that human stefin B exhibits molten globule intermediates when denatured by acid or GuHCl. In the presence of TFE, it transforms into a highly helical state. In our first study on its folding mechanism (Z Λerovnik et al., Proteins 32:296-303), the kinetics measured by circular dich
Elucidating the properties of the denatured state of proteins under conditions relevant for their folding is a key factor in understanding the folding process. We show that a peptide corresponding to residues 111-120 of human β£-lactalbumin has a pronounced propensity to adopt nonnative structure in
of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR ## SYNOPSIS Binding of the hydrophobic fluorescent probe, 1-anilino-naphthalene-8-sulfonate ( ANS) , to synthetic polypeptides and proteins with a different structural organization has been studied. It has been shown that ANS has a mu
All possible protein folding intermediates exist in equilibrium with the native protein at native as well as non-native conditions, with occupation determined by their free energy level. The study of these forms can illuminate the fundamental principles of protein structure and folding. Hydrogen exc